Bio-sensing Using Cell Surface Display: Principles and Variations of a Cell Sensor

2019 ◽  
pp. 93-106 ◽  
Author(s):  
Seiji Shibasaki
2022 ◽  
Vol 61 ◽  
pp. 102570
Author(s):  
João Vitor Dutra Molino ◽  
Roberta Carpine ◽  
Karl Gademann ◽  
Stephen Mayfield ◽  
Simon Sieber

2014 ◽  
Vol 7 (334) ◽  
pp. rs4-rs4 ◽  
Author(s):  
H. Onuma ◽  
T. Komatsu ◽  
M. Arita ◽  
K. Hanaoka ◽  
T. Ueno ◽  
...  

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Alexander Braun ◽  
Matthew J. Farber ◽  
Zachary A. Klase ◽  
Peter B. Berget ◽  
Kenneth A. Myers

1994 ◽  
Vol 126 (4) ◽  
pp. 979-989 ◽  
Author(s):  
S Corvera ◽  
A Chawla ◽  
R Chakrabarti ◽  
M Joly ◽  
J Buxton ◽  
...  

The unique COOH-terminal 30-amino acid region of the adipocyte/skeletal muscle glucose transporter (GLUT4) appears to be a major structural determinant of this protein's perinuclear localization, from where it is redistributed to the cell surface in response to insulin. To test whether an underlying mechanism of this domain's function involves glucose transporter endocytosis rates, transfected cells were generated expressing exofacial hemagglutinin epitope (HA)-tagged erythrocyte/brain glucose transporter (GLUT1) or a chimera containing the COOH-terminal 30 amino acids of GLUT4 substituted onto this GLUT1 construct. Incubation of COS-7 or CHO cells expressing the HA-tagged chimera with anti-HA antibody at 37 degrees resulted in an increased rate of antibody internalization compared to cells expressing similar levels of HA-tagged GLUT1, which displays a cell surface disposition. Colocalization of the internalized anti-HA antibody in vesicular structures with internalized transferrin and with total transporters was established by digital imaging microscopy, suggesting the total cellular pool of transporters are continuously recycling through the coated pit endocytosis pathway. Mutation of the unique double leucines 489 and 490 in the rat GLUT4 COOH-terminal domain to alanines caused the HA-tagged chimera to revert to the slow endocytosis rate and steady-state cell surface display characteristic of GLUT1. These results support the hypothesis that the double leucine motif in the GLUT4 COOH terminus operates as a rapid endocytosis and retention signal in the GLUT4 transporter, causing its localization to intracellular compartments in the absence of insulin.


2008 ◽  
Vol 74 (11) ◽  
pp. 3342-3348 ◽  
Author(s):  
Masayoshi Tanaka ◽  
Yuko Nakata ◽  
Tetsushi Mori ◽  
Yoshiko Okamura ◽  
Hitoshi Miyasaka ◽  
...  

ABSTRACT Bacterial cell surface display is a widely used technology for bioadsorption and for the development of a variety of screening systems. Magnetotactic bacteria are unique species of bacteria due to the presence of magnetic nanoparticles within them. These intracellular, nanosized (50 to 100 nm) magnetic nanoparticles enable the cells to migrate and be manipulated by magnetic force. In this work, using this unique characteristic and based on whole-genomic and comprehensive proteomic analyses of these bacteria, a cell surface display system has been developed by expressing hexahistidine residues within the outer coiled loop of the membrane-specific protein (Msp1) of the “Magnetospirillum magneticum” (proposed name) AMB-1 bacterium. The optimal display site of the hexahistidine residues was successfully identified via secondary structure prediction, immunofluorescence microscopy, and heavy metal binding assay. The established AMB-1 transformant showed high immunofluorescence response, high Cd2+ binding, and high recovery efficiency in comparison to those of the negative control when manipulated by magnetic force.


2009 ◽  
Vol 76 (3) ◽  
pp. 971-973 ◽  
Author(s):  
Jong Hwan Baek ◽  
Mee-Jung Han ◽  
Seung Hwan Lee ◽  
Sang Yup Lee

ABSTRACT A cell surface display system was developed using Escherichia coli OmpC as an anchoring motif. The fused Pseudomonas fluorescens SIK W1 lipase was successfully displayed on the surface of E. coli cells, and the lipase activity could be enhanced by the coexpression of the gadBC genes identified by transcriptome analysis.


2011 ◽  
Vol 347-353 ◽  
pp. 3635-3640 ◽  
Author(s):  
Jian Zhang Lu ◽  
Qin Guo ◽  
Mei Lin Cui ◽  
Lu Yang ◽  
Shan Shan Du ◽  
...  

Laccases (1.10.3.2, p-diphenol: dioxygen oxidoreductases) is a family of blue copper-containing oxidases that are commonly found in bacteria, fungi and plants. It is able to oxidize and degrade a variety of aromatic compounds and other organic compounds. Due to this ability, laccases can serve environmental bioremediation processes and industrial purposes. Cell-surface display of enzymes is one of the most attractive applications in yeast. It is a effective utilization to construct the whole cell biocatalyst. The cDNA sequence of Trametes sp. C30 LAC3 was optimized and synthesized according to the codon bias of Saccharomyces Italic textcerevisiae, because codon optimization has been proved to be effective to maximize production of heterologous proteins in yeast. The genes encoding galactokinase (GAL1) promoter, α-mating factor 1 (MFα1) pre-pro secretion signal, fully codon-optimized LAC3, the 320 amino acids of C terminal of α-agglutinin, alcohol dehydrogenase (ADH1) terminator and kanMX cassette were amplified and cloned into YEplac181 to construct a cell-surface display vector called pGMAAK-lac3 with α-agglutinin as an anchor. Then pGMAAK-lac3 was transformed into S. cerevisiae. The results show LAC3 was immobilized and actively expressed on S. cerevisiae. However, the substrate specifity and activity were obviously changed. The displayed LAC3 lost the activity to phenolic substrate (guaiacol) and its activity to non-phenolic substrate (ABTS) was greatly reduced. To our knowledge, this was the first attempt to construct and express laccase through cell-surface display technology.


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